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Article

The role of cysteine residues in the transport of mercuric ions by the Tn501 MerT and MerP mercury-resistance proteins.

Molecular microbiology - 1 Jul 1995

Morby A P, Hobman J L, Brown N L

Abstract excerpt

Each cysteine residue in the MerT and MerP polypeptides of bacterial transposon Tn501 was replaced by serine, and the mercury-resistance phenotypes of the mutants were determined in Escherichia coli. Cys-24 and Cys-25 in the first transmembrane region of MerT were essential for transport of mercuric ions through the cytoplasmic membrane, and mutations Cys-76-Ser, Cys-82-Ser or Gly-38-Asp in MerT or Cys-36-Ser in...

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Identifiers

PMID: 7476206
DOI: 10.1111/j.1365-2958.1995.mmi_17010025.x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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The role of cysteine residues in the transport of mercuric ions by the Tn501 MerT and MerP mercury-resistance proteins.PMID 7476206Read ↗

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Mutations in dsbA and dsbB, but not dsbC, lead to an enhanced sensitivity of Escherichia coli to Hg2+ and Cd2+.Semantic proximity Read ↗

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